Topoisomerase

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**[[1s14]] – EcTOPIV ParE<br />
**[[1s14]] – EcTOPIV ParE<br />
**[[1s16]] - EcTOPIV ParE+ADPNP<br />
**[[1s16]] - EcTOPIV ParE+ADPNP<br />
-
**[[3ltn]], [[3k9f]], [[3ksb]], [[3rad]], [[3rae]], [[3raf]], [[4i3h]], [[4juo]] - SpTOPIV subunit A+B+DNA<br />
+
**[[3ltn]], [[3k9f]], [[3ksb]], [[3rad]], [[3rae]], [[3raf]], [[4i3h]], [[4juo]], [[4koe]] - SpTOPIV subunit A+B+DNA<br />
 +
**[[4koe]], [[4kpe]] - SpTOPIV subunit A+B (mutant) +DNA<br />
**[[3foe]], [[3fof]] - SpTOPIV subunit A+B+DNA+quinolone<br />
**[[3foe]], [[3fof]] - SpTOPIV subunit A+B+DNA+quinolone<br />
**[[2nov]] - SpTOPIV subunit A<br />
**[[2nov]] - SpTOPIV subunit A<br />
**[[4em7]], [[4emv]], [[4lp0]], [[4lpb]], [[4mb9]], [[4mbc]], [[4mot]] - SpTOPIV subunit B + inhibitor<br />
**[[4em7]], [[4emv]], [[4lp0]], [[4lpb]], [[4mb9]], [[4mbc]], [[4mot]] - SpTOPIV subunit B + inhibitor<br />
-
**[[2inr]] - TOPIV subunit A – ''Staphylococcus aureus''<br />
+
**[[2inr]] - SaTOPIV subunit A – ''Staphylococcus aureus''<br />
 +
**[[4url]], [[4urn]] - SaTOPIV subunit B N terminal + antibiotic<br />
**[[1wp5]] – TOPIV C-terminal – ''Geobacillus stearothermophilus''<br />
**[[1wp5]] – TOPIV C-terminal – ''Geobacillus stearothermophilus''<br />
**[[2xkj]] – AbTOPIV pare+parc subunits – ''Acinetobacter baumannii''<br />
**[[2xkj]] – AbTOPIV pare+parc subunits – ''Acinetobacter baumannii''<br />

Revision as of 07:53, 21 June 2015

Image:2f4q.png
Crystal Structure of Topoisomerase 2f4q

Template:STRUCTURE 2h7f












Topoisomerase (TOP) winds and unwinds DNA double helix in order to enable DNA replication.

  • TOPI cuts one strand of the double helix. It has 3 subclasses: TOPIA which shares its mechanism with TOPII and TOPIB which uses rotary mechanism and includes topo I and topo III. TOPIC called TOPV shares its mechanism with TOPIB but is structurally unique.
  • TOPII cuts both strands of the double helix. Its subclasses are TOPIIA including topo II and TOPIIB which includes topo VI.
  • TOPIV is a type of TOPII, contains an ATP-binding domain ParE and a catalytic domain ParC.

See also Variola Topoisomerase 1B.

Contents

Function

The reaction catalyzed by topoisomerases leads to the conversion of one topological isomer of DNA to another. TOP3 is a potent decatenase.

GO Annotations

Database ID Symbol Qualifier GO Identifier GO Term Name Aspect Evidence Reference With Taxon Date Assigned by Product Form ID
UniProtKB P14294 topB GO:0006259 DNA metabolic process P IEA InterPro2GO InterPro:IPR006154 83333 20101127 InterPro
UniProtKB P14294 topB GO:0006265 DNA topological change P IEA InterPro2GO InterPro:IPR000380 83333 20101127 InterPro
UniProtKB P14294 topB GO:0006265 DNA topological change P IEA InterPro2GO InterPro:IPR003601 83333 20101127 InterPro
UniProtKB P14294 topB GO:0006265 DNA topological change P IEA InterPro2GO InterPro:IPR003602 83333 20101127 InterPro
UniProtKB P14294 topB GO:0006265 DNA topological change P IEA InterPro2GO InterPro:IPR005738 83333 20101127 InterPro
UniProtKB P14294 topB GO:0006265 DNA topological change P IEA InterPro2GO InterPro:IPR013497 83333 20101127 InterPro
UniProtKB P14294 topB GO:0006265 DNA topological change P IEA InterPro2GO InterPro:IPR013824 83333 20101127 InterPro
UniProtKB P14294 topB GO:0006265 DNA topological change P IEA InterPro2GO InterPro:IPR013825 83333 20101127 InterPro
UniProtKB P14294 topB GO:0006268 DNA unwinding involved in replication P IEA InterPro2GO InterPro:IPR013824 83333 20101127 InterPro
UniProtKB P14294 topB GO:0006268 DNA unwinding involved in replication P IEA InterPro2GO InterPro:IPR013825 83333 20101127 InterPro
UniProtKB P14294 topB GO:0000166 nucleotide binding F IEA Swiss-Prot Keywords2GO SP_KW:KW-0547 83333 20101127 UniProtKB
UniProtKB P14294 topB GO:0003676 nucleic acid binding F IEA InterPro2GO InterPro:IPR006154 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003677 DNA binding F IEA InterPro2GO InterPro:IPR000380 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003677 DNA binding F IEA InterPro2GO InterPro:IPR003601 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003677 DNA binding F IEA InterPro2GO InterPro:IPR003602 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003677 DNA binding F IEA InterPro2GO InterPro:IPR005738 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003677 DNA binding F IEA InterPro2GO InterPro:IPR013497 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003677 DNA binding F IEA InterPro2GO InterPro:IPR013824 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003677 DNA binding F IEA InterPro2GO InterPro:IPR013825 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003677 DNA binding F IEA Swiss-Prot Keywords2GO SP_KW:KW-0238 83333 20101127 UniProtKB
UniProtKB P14294 topB GO:0003916 DNA topoisomerase activity F IEA InterPro2GO InterPro:IPR003601 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003916 DNA topoisomerase activity F IEA InterPro2GO InterPro:IPR003602 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003916 DNA topoisomerase activity F IEA InterPro2GO InterPro:IPR005738 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003916 DNA topoisomerase activity F IEA InterPro2GO InterPro:IPR013497 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003916 DNA topoisomerase activity F IEA InterPro2GO InterPro:IPR013824 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003916 DNA topoisomerase activity F IEA InterPro2GO InterPro:IPR013825 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003916 DNA topoisomerase activity F IEA Swiss-Prot Keywords2GO SP_KW:KW-0799 83333 20101127 UniProtKB
UniProtKB P14294 topB GO:0003917 DNA topoisomerase type I activity F IDA PMID:6326814 83333 20100621 EcoliWiki
UniProtKB P14294 topB GO:0003917 DNA topoisomerase type I activity F IEA InterPro2GO InterPro:IPR000380 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003917 DNA topoisomerase type I activity F IEA EC2GO EC:5.99.1.2 83333 20100703 UniProtKB
UniProtKB P14294 topB GO:0005515 protein binding F IPI PMID:15690043 frlR (FRLR_ECOLI) 83333 20101127 IntAct
UniProtKB P14294 topB GO:0005524 ATP binding F IEA Swiss-Prot Keywords2GO SP_KW:KW-0067 83333 20101127 UniProtKB
UniProtKB P14294 topB GO:0016853 isomerase activity F IEA Swiss-Prot Keywords2GO SP_KW:KW-0413 83333 20101127 UniProtKB
UniProtKB P14294 topB GO:0005694 chromosome C IEA InterPro2GO InterPro:IPR000380 83333 20101127 InterPro
UniProtKB P14294 topB GO:0005694 chromosome C IEA InterPro2GO InterPro:IPR003601 83333 20101127 InterPro
UniProtKB P14294 topB GO:0005694 chromosome C IEA InterPro2GO InterPro:IPR003602 83333 20101127 InterPro
UniProtKB P14294 topB GO:0005694 chromosome C IEA InterPro2GO InterPro:IPR005738 83333 20101127 InterPro
UniProtKB P14294 topB GO:0005694 chromosome C IEA InterPro2GO InterPro:IPR013497 83333 20101127 InterPro
UniProtKB P14294 topB GO:0005694 chromosome C IEA InterPro2GO InterPro:IPR013824 83333 20101127 InterPro
UniProtKB P14294 topB GO:0005694 chromosome C IEA InterPro2GO InterPro:IPR013825 83333 20101127 InterPro

Copied from [1] Last updated Dec 2 2010


3D Structures of Topoisomerase

Updated on 21-June-2015


Created with the participation of Sonny Zhao.

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Joel L. Sussman, Alexander Berchansky, Jaime Prilusky

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